Encapsulation of l-valine, d-leucine and d-methionine by cucurbit[8]uril

Zhang, Zeng Hui; Lin, Rui Lian; Yu, Xiang Yun; Chen, Li Xia; Tao, Zhu; Xiao, Xin; Wei, Gang; Redshaw, Carl; Liu, Jing Xin

Abstract

The binding interactions of cucurbit[8]uril (Q[8]) with L-valine, D-leucine, and D-methionine, both in aqueous solution and solid state, have been studied by 1H NMR spectroscopy and X-ray crystallography. 1H NMR data indicate that Q[8] can encapsulate these three kinds of amino acids in aqueous solution. X-ray crystallography reveals how the Q[8] binds with the amino acids to form inclusion complexes L-Val2@Q[8], D-Leu2@Q[8], and D-Met2@Q[8] through host-guest interactions. It was also found that the deformation degree of the Q[8] host is related to the molecular size of the encapsulated guests.

Citation

Zhang, Z. H., Lin, R. L., Yu, X. Y., Chen, L. X., Tao, Z., Xiao, X., …Liu, J. X. (2022). Encapsulation of l-valine, d-leucine and d-methionine by cucurbit[8]uril. CrystEngComm, 24(5), 1035-1040. https://doi.org/10.1039/d1ce01513c

• Journal Article Type: Article
• Acceptance Date: Jan 4, 2022
• Online Publication Date: Jan 4, 2022
• Publication Date: Feb 7, 2022
• Deposit Date: Jan 15, 2022
• Publicly Available Date: Jan 5, 2023
• Journal: CrystEngComm
• Electronic ISSN: 1466-8033
• Publisher: Royal Society of Chemistry
• Peer Reviewed: Peer Reviewed
• Volume: 24
• Issue: 5
• Pages: 1035-1040
• DOI: https://doi.org/10.1039/d1ce01513c
• Keywords: Condensed Matter Physics; General Materials Science; General Chemistry
• Public URL: https://hull-repository.worktribe.com/output/3913336